1fin: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fin OCA], [http://www.ebi.ac.uk/pdbsum/1fin PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fin RCSB]</span>
}}
}}


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[[Category: Pavletich, N P.]]
[[Category: Pavletich, N P.]]
[[Category: Russo, A A.]]
[[Category: Russo, A A.]]
[[Category: ATP]]
[[Category: cdk]]
[[Category: cdk]]
[[Category: complex (transferase/cyclin)]]
[[Category: complex (transferase/cyclin)]]
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[[Category: phosphorylation]]
[[Category: phosphorylation]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:47:33 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:23:38 2008''

Revision as of 20:23, 30 March 2008

File:1fin.jpg


PDB ID 1fin

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEX


OverviewOverview

The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 A resolution. CyclinA binds to one side of CDK2's catalytic cleft, inducing large conformational changes in its PSTAIRE helix and T-loop. These changes activate the kinase by realigning active site residues and relieving the steric blockade at the entrance of the catalytic cleft.

About this StructureAbout this Structure

1FIN is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex., Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massague J, Pavletich NP, Nature. 1995 Jul 27;376(6538):313-20. PMID:7630397

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